On the potential alternate binding change mechanism in a dimeric structure of Pyruvate Phosphate Dikinase.

ABSTRACT: The pyruvate phosphate dikinase (PPDK) reaction mechanism is characterized by a distinct spatial separation of reaction centers and large conformational changes involving an opening-closing motion of the nucleotide-binding domain (NBD) and a swiveling motion of the central domain (CD). However, why PPDK is active only in a dimeric form and to what extent an alternate binding change mechanism could underlie this fact has remained elusive. We performed unbiased molecular dynamics simulations, configurational free energy computations, and rigidity analysis to address this question. Our results support the hypothesis that PPDK dimerization influences the opening-closing motion of the NBDs, and that this influence is mediated via the CDs of both chains. Such an influence would be a prerequisite

SUBMITTER: Ciupka D 

PROVIDER: S-EPMC5556012 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature